1E5W
Structure of isolated FERM domain and first long helix of moesin
Summary for 1E5W
| Entry DOI | 10.2210/pdb1e5w/pdb |
| Related | 1EF1 |
| Descriptor | MOESIN (2 entities in total) |
| Functional Keywords | membrane protein, moesin, ferm, erm |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P26038 |
| Total number of polymer chains | 1 |
| Total formula weight | 41054.31 |
| Authors | Edwards, S.D.,Keep, N.H. (deposition date: 2000-08-03, release date: 2001-06-27, Last modification date: 2024-05-08) |
| Primary citation | Edwards, S.D.,Keep, N.H. The 2.7 A Crystal Structure of the Activated Ferm Domain of Moesin: An Analysis of Structural Changes on Activation Biochemistry, 40:7061-, 2001 Cited by PubMed Abstract: Moesin binds to a large range of proteins through its N terminal FERM (band 4.1, ezrin, radixin, moesin) domain. In full-length moesin isolated from cells, this binding is masked by binding to the C-terminal domain of moesin (C-ERMAD). Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which releases the C-ERMAD. A recently determined crystal structure of a noncovalent complex of the FERM and C-ERMAD domains showed for the first time that the structure of the FERM domain consists of three subdomains, each of which is similar to known structures. The structure reported here also contains a unique 47-residue helix pointing away from the FERM domain at the start of the alpha domain, in agreement with secondary structure predictions. Removal of the C-ERMAD does not result in a huge rearrangement of the FERM domain, but comparison with the activated radixin structure shows a consistent set of small changes. Not surprisingly, the exposed C-ERMAD binding area interacts in crystal contacts. More interestingly, a negatively charged peptide binds to the inositol site in a crystal contact and causes a greater conformational change in the structure than inositol. PubMed: 11401550DOI: 10.1021/BI010419H PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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